PDBsum entry 1h0r

Dehydratase

PDB id: 1h0r

Contents

Protein chain

139 a.a. *

Ligands

FA1

PO4

GOL

Metals

_CL ×2

Waters ×153

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Structural basis for selectivity of oxime based inhibitors towards type ii dehydroquinase from mycobacterium tuberculosis

Authors

D.A.Robinson, A.W.Roszak, M.Frederickson, C.Abell, J.R.Coggins, A.J.Lapthorn.

Ref.

To be Published ...

Secondary reference #1

Title

The two types of 3-Dehydroquinase have distinct structures but catalyze the same overall reaction.

Authors

D.G.Gourley, A.K.Shrive, I.Polikarpov, T.Krell, J.R.Coggins, A.R.Hawkins, N.W.Isaacs, L.Sawyer.

Ref.

Nat Struct Biol, 1999, 6, 521-525. [DOI no: 10.1038/9287]

PubMed id

10360352

Figure 2.
Figure 2. Stereodiagrams of the electron density maps for the types I and II 3-dehydroquinase. a, A view of the active site region within the -barrel, looking into the site from the more open end of the barrel. The electron density map (2F[o] - F[c]) calculated at 2.7 Å resolution is noncrystallographically averaged and solvent flattened and contoured at 1 . The bound product is attached to Lys 170 at the C-3 position. The substrate-interacting residues Gln 236, Ser 232, Glu 46, Arg 48 and Arg 82 arise from the -strands and the loop regions of the C-terminal end of the strands, whereas Arg 213 is located on the G helix. The water molecule W1, which interacts with the C-4 hydroxyl group and the Schiff base nitrogen of Lys 170, is also shown. b, A view of the region around His 132 showing the typical quality of the (2F[o] - F[c]) electron density map for the type II 3-dehydroquinase. There is no significant electron density for residues in the loop between Arg 18 and Gly 25.

Figure 3.
Figure 3. The structure of an enzyme subunit. a, A cartoon of the type I DHQase from Salmonella typhi, looking into the parallel / barrel. The product 3-dehydroshikimate is shown in the center of the molecule with the position of the imine-forming Lys 170 to which it is covalently attached, and the conserved side-chains involved in ligand binding, also shown. b, A stereodiagram of the C trace of the type I DHQase subunit. c, A cartoon of the type II DHQase from Mycobacterium tuberculosis; residues 19−24 were not included in the molecular structure since there was insufficient electron density, indicating that this region is disordered. d, A stereo diagram of the C trace of the type II DHQase subunit. The diagrams were prepared using MOLSCRIPT^40.

The above figures are reproduced from the cited reference with permission from Macmillan Publishers Ltd